The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
The zona pellucida is an extracellular matrix that surrounds the oocyte and early embryo. It is composed primarily of three or four glycoproteins with various functions during fertilization and preimplantation development. The protein encoded by this gene is a structural component of the zona pellucida and functions in secondary binding and penetration of acrosome-reacted spermatozoa. The nascent protein contains a N-terminal signal peptide sequence, a conserved ZP domain, a consensus furin cleavage site, and a C-terminal transmembrane domain. It is hypothesized that furin cleavage results in release of the mature protein from the plasma membrane for subsequent incorporation into the zona pellucida matrix. However, the requirement for furin cleavage in this process remains controversial based on mouse studies.
Protein Aliases: Processed zona pellucida sperm-binding protein 2; zona pellucida 2 glycoprotein; Zona pellucida glycoprotein 2; zona pellucida glycoprotein 2 (sperm receptor); zona pellucida glycoprotein ZP2; Zona pellucida protein A; Zona pellucida sperm-binding protein 2; Zp-2
Gene Aliases: Zp-2; ZP2; ZPA